Structure of the Reaction Center from Rhodopseudomonas sphaeroides R-26 and 2.4.1: Symmetry Relations and Sequence Comparisons between Different Species

Komiya, H. and Yeates, T. O. and Rees, D. C. and Allen, J. P. and Feher, G.
(1988)
Structure of the Reaction Center from Rhodopseudomonas sphaeroides R-26 and 2.4.1: Symmetry Relations and Sequence Comparisons between Different Species.
Proceedings of the National Academy of Sciences of the United States of America, 85
(23).
pp. 9012-9016.
ISSN 0027-8424.
PMCID PMC282652.
https://resolver.caltech.edu/CaltechAUTHORS:20150209-103422026

Abstract

Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, which relates both the cofactors and the L and M subunits. For the reaction center from Rhodobacter sphaeroides, deviations from this twofold symmetry axis have been quantitated by superposing, by a 180 degrees rotation, the cofactors of the B branch onto the A branch and the M subunit onto the L subunit. An alignment of the sequences of the L and M subunits from four purple bacteria, one green bacterium, and the D_1 and D_2 subunits of a photosystem II-containing green alga is presented. The residues that are conserved in all six species are shown in relation to the structure of Rb. sphaeroides and their possible role in the function of the reaction center is discussed. A method is presented for characterizing the exposure of α-helices to the membrane based on the periodicity of conserved residues. This method may prove useful for modeling the three-dimensional structures of membrane proteins.